Biochemistry and Biophysics Reports (Sep 2023)

Alterations in mitochondrial protein glycosylation in myocardial ischaemia reperfusion injury

  • Xinyu Feng,
  • Qing Shi,
  • Qiang Jian,
  • Fan Li,
  • Zheng Li,
  • Kang Cheng

Journal volume & issue
Vol. 35
p. 101509

Abstract

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The alterations in mitochondrial protein glycosylation in myocardial ischaemia reperfusion (I/R) injury are still unclear. Therefore, based on a lectin microarray and liquid chromatograph-mass spectrometer/mass spectrometer (LC‒MS/MS) technology combined with a bioinformatics analysis, we studied the changes in mitochondrial protein glycosylation during I/R injury. This study revealed significant differences in mitochondrial glycoprotein during I/R injury. Compared with the sham operation group, the model group, which underwent ischaemia for 30 min, showed a high expression of glycan structures recognized by lectins, such as WFA, PTL-I, LTL, GSL-I, SBA and SNA, and a low expression of glycan structures recognized by ConA, VVA and RCA120. The model group, which underwent ischaemia for 45 min, showed a high expression of glycan structures recognized by LTL and SNA and a low expression of glycan structures recognized by ECA. Further analysis showed that the Siaα2-6Gal/N-acetylgalactosamine (GalNAc) structures recognized by SNA were significantly increased. In total, 91 differential proteins were identified by LC‒MS/MS, and 8 hub genes were screened by Gene Ontology (GO) enrichment, Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment and protein interaction analyses. Compared with the Gene Expression Omnibus (GEO) database genes, two differential genes, Pros1 and Vtn, were obtained. Pros1 is a key regulator of the inflammatory response and vascular injury response. The Vtn gene variant is associated with the risk of myocardial infarction. This study is expected to provide a new method for the treatment of I/R injury and could provide new ideas for the postoperative prognosis of patients.

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